1kr7: Difference between revisions

Line 4:

==Overview==

A very short hemoglobin (CerHb; 109 amino acids) binds O(2) cooperatively, in the nerve tissue of the nemertean worm Cerebratulus lacteus to sustain, neural activity during anoxia. Sequence analysis suggests that CerHb, tertiary structure may be unique among the known globin fold evolutionary, variants. The X-ray structure of oxygenated CerHb (R factor 15.3%, at 1.5, A resolution) displays deletion of the globin N-terminal A helix, an, extended GH region, a very short H helix, and heme solvent shielding based, on specific aromatic residues. The heme-bound O(2) is stabilized by, hydrogen bonds to the distal TyrB10-GlnE7 pair. Ligand access to heme may, take place through a wide protein matrix tunnel connecting the distal site, to a surface cleft located between the E and H helices.

A very short hemoglobin (CerHb; 109 amino acids) binds O(2) cooperatively in the nerve tissue of the nemertean worm Cerebratulus lacteus to sustain neural activity during anoxia. Sequence analysis suggests that CerHb tertiary structure may be unique among the known globin fold evolutionary variants. The X-ray structure of oxygenated CerHb (R factor 15.3%, at 1.5 A resolution) displays deletion of the globin N-terminal A helix, an extended GH region, a very short H helix, and heme solvent shielding based on specific aromatic residues. The heme-bound O(2) is stabilized by hydrogen bonds to the distal TyrB10-GlnE7 pair. Ligand access to heme may take place through a wide protein matrix tunnel connecting the distal site to a surface cleft located between the E and H helices.

==About this Structure==

Line 20:

[[Category: Nardini, M.]]

[[Category: Pesce, A.]]

[[Category: Riggs, A.F.]]

[[Category: Riggs, A F.]]

[[Category: Yamauchi, k.]]

[[Category: ACT]]

Line 31:

[[Category: protein cavities]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 16~~:15:06 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:37:06 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==Overview==
-A very short hemoglobin (CerHb; 109 amino acids) binds O(2) cooperatively, in the nerve tissue of the nemertean worm Cerebratulus lacteus to sustain, neural activity during anoxia. Sequence analysis suggests that CerHb, tertiary structure may be unique among the known globin fold evolutionary, variants. The X-ray structure of oxygenated CerHb (R factor 15.3%, at 1.5, A resolution) displays deletion of the globin N-terminal A helix, an, extended GH region, a very short H helix, and heme solvent shielding based, on specific aromatic residues. The heme-bound O(2) is stabilized by, hydrogen bonds to the distal TyrB10-GlnE7 pair. Ligand access to heme may, take place through a wide protein matrix tunnel connecting the distal site, to a surface cleft located between the E and H helices.
+A very short hemoglobin (CerHb; 109 amino acids) binds O(2) cooperatively in the nerve tissue of the nemertean worm Cerebratulus lacteus to sustain neural activity during anoxia. Sequence analysis suggests that CerHb tertiary structure may be unique among the known globin fold evolutionary variants. The X-ray structure of oxygenated CerHb (R factor 15.3%, at 1.5 A resolution) displays deletion of the globin N-terminal A helix, an extended GH region, a very short H helix, and heme solvent shielding based on specific aromatic residues. The heme-bound O(2) is stabilized by hydrogen bonds to the distal TyrB10-GlnE7 pair. Ligand access to heme may take place through a wide protein matrix tunnel connecting the distal site to a surface cleft located between the E and H helices.
 ==About this Structure==
@@ Line 20: / Line 20: @@
 [[Category: Nardini, M.]]
 [[Category: Pesce, A.]]
-[[Category: Riggs, A.F.]]
+[[Category: Riggs, A F.]]
 [[Category: Yamauchi, k.]]
 [[Category: ACT]]
@@ Line 31: / Line 31: @@
 [[Category: protein cavities]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:15:06 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:37:06 2008''